1.14.13.20: 2,4-dichlorophenol 6-monooxygenase
This is an abbreviated version!
For detailed information about 2,4-dichlorophenol 6-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.20
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1.14.13.20
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2,4-dichlorophenoxyacetic
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chlorocatechols
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3,5-dichlorocatechol
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fad
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chlorophenols
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catechols
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alcaligenes
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eutrophus
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2,4-d-degradative
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ortho-substituted
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3-chlorophenol
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maleylacetate
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alpha-2
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polychlorinated
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4-chlorocatechol
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cycloisomerase
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biphenyl-contaminated
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chemotaxonomic
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3-chloro
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chloromuconate
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non-substrate
- 1.14.13.20
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2,4-dichlorophenoxyacetic
- chlorocatechols
- 3,5-dichlorocatechol
- fad
- chlorophenols
- catechols
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alcaligenes
- eutrophus
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2,4-d-degradative
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ortho-substituted
- 3-chlorophenol
- maleylacetate
- alpha-2
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polychlorinated
- 4-chlorocatechol
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cycloisomerase
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biphenyl-contaminated
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chemotaxonomic
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3-chloro
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chloromuconate
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non-substrate
Reaction
Synonyms
2,4-DCP hydroxylase, 2,4-dichlorophenol hydroxylase, 2,4-dichlorophenol monooxygenase, chlorophenol hydroxylase, DCM, oxygenase, 2,4-dichlorophenol 6-mono, oxygenase, 2,4-dichlorophenol mono-, phenol hydroxylase, tfdB, TfdB-JLU
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1.14.13.20 2,4-dichlorophenol 6-monooxygenaseAdvanced search results
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General Information on EC 1.14.13.20 - 2,4-dichlorophenol 6-monooxygenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
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analysis of substrate binding by the mutant P316Q and the wild-type enzyme, docking study, overview
metabolism
physiological function
additional information
metabolism
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the enzyme is involved in degradation of the herbicide 2,4-dichlorophenoxyacetic acid
metabolism
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the enzyme is involved in the catabolism of 2,4-dichlorophenol, pathways, overview
metabolism
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two dcm gene clusters essential for the degradation of diclofop-methyl in a microbial consortium of Rhodococcus sp. JT-3 and Brevundimonas sp. JT-9
metabolism
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two dcm gene clusters essential for the degradation of diclofop-methyl in a microbial consortium of Rhodococcus sp. JT-3 and Brevundimonas sp. JT-9
metabolism
Bacillus licheniformis MTCC 25059
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the enzyme is involved in the catabolism of 2,4-dichlorophenol, pathways, overview
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metabolism
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the enzyme is involved in the catabolism of 2,4-dichlorophenol, pathways, overview
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physiological function
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2,4-dichlorophenol hydroxylase (2,4-DCP hydroxylase) is a key enzyme in the degradation of 2,4-dichlorophenoxyacetic acid through the hydroxylation step in many bacteria
physiological function
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degradation of 2,4-dichlorophenol (2,4-DCP) by phenol adapted bacterium Bacillus licheniformis strain SL10 (MTCC 25059) at a relatively fast rate. The organism exhibits tolerance to 150 ppm of 2,4-DCP and shows a linear relationship between the growth and substrate concentration, the inhibitory concentration is 55.74 mg/l, kinetics, overview. The degradation efficiency of the organism is 74% under optimum conditions but increases to 97% when the growth medium contains nil sodium chloride. The organism follows a meta-cleavage pathway while degrading 2,4-DCP
physiological function
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the consortium L1 of Rhodococcus sp. JT-3 and Brevundimonas sp. JT-9 is able to degrade diclofop-methyl (DCM) through a synergistic metabolism, molecular mechanism of DCM degradation, overview. DCM is initially transformed by strain JT-3 to diclofop acid and then by strain JT-9 to 2-(4-hydroxyphenoxy) propionic acid as well as 2,4-dichlorophenol (DCP). DCP is the first intermediate during the degradation of herbicide 2,4-dichlorophenoxyacetic acid (2,4-D), wherein 2,4-D is converted into 3,5-dichlorocatechol by the 2,4-dichlorophenol hydroxylase
physiological function
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the consortium L1 of Rhodococcus sp. JT-3 and Brevundimonas sp. JT-9 is able to degrade diclofop-methyl (DCM) through a synergistic metabolism, molecular mechanism of DCM degradation, overview. DCM is initially transformed by strain JT-3 to diclofop acid and then by strain JT-9 to 2-(4-hydroxyphenoxy) propionic acid as well as 2,4-dichlorophenol (DCP). DCP is the first intermediate during the degradation of herbicide 2,4-dichlorophenoxyacetic acid (2,4-D), wherein 2,4-D is converted into 3,5-dichlorocatechol by the 2,4-dichlorophenol hydroxylase
physiological function
Bacillus licheniformis MTCC 25059
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degradation of 2,4-dichlorophenol (2,4-DCP) by phenol adapted bacterium Bacillus licheniformis strain SL10 (MTCC 25059) at a relatively fast rate. The organism exhibits tolerance to 150 ppm of 2,4-DCP and shows a linear relationship between the growth and substrate concentration, the inhibitory concentration is 55.74 mg/l, kinetics, overview. The degradation efficiency of the organism is 74% under optimum conditions but increases to 97% when the growth medium contains nil sodium chloride. The organism follows a meta-cleavage pathway while degrading 2,4-DCP
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physiological function
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degradation of 2,4-dichlorophenol (2,4-DCP) by phenol adapted bacterium Bacillus licheniformis strain SL10 (MTCC 25059) at a relatively fast rate. The organism exhibits tolerance to 150 ppm of 2,4-DCP and shows a linear relationship between the growth and substrate concentration, the inhibitory concentration is 55.74 mg/l, kinetics, overview. The degradation efficiency of the organism is 74% under optimum conditions but increases to 97% when the growth medium contains nil sodium chloride. The organism follows a meta-cleavage pathway while degrading 2,4-DCP
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additional information
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molecular docking experiments of the enzyme TfdB-JLU's homology model with its natural substrate 2,4-dichlorophenol (with template PDB ID 5brt) reveals that the phenyl rings of 2,4-DCP form strong interactions with residues His47, Ile48, Trp222, Pro316, and Phe424. These residues are found to be important for substrate binding in the active site
additional information
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synthesis of hybrid nanoflowers (hNFs) formed from cold-adapted 2,4-dichlorophenol hydroxylase (tfdBJLU) and Cu3(PO4)2 x 3H2O. Analysis of the influence of experimental factors, such as the pH of the solution mixture and the enzyme and Cu2+ concentrations, on the activity of the prepared tfdB-JLU-hNFs. 200 mM is the optimal Cu2+ concentration to get tfdB-JLU-hNFs with highest activity recovery, method optimization, overview. The tfdB-JLU-hNFs exhibit excellent durability with 58.34% residual activity after six successive cycles, and up to 90.58% residual activity after 20 days of storage. This multistage and hierarchical flower-like structure can effectively increase enzyme activity and stability with respect to those of the free enzyme. The satisfactory removal rate of 2,4-dichlorophenol catalyzed by tfdB-JLU-hNFs suggests that this immobilized enzyme exhibits great potential for application in bioremediation
